CA2249409A1 - Iga1 protease fragment as carrier peptide - Google Patents
Iga1 protease fragment as carrier peptideInfo
- Publication number
- CA2249409A1 CA2249409A1 CA002249409A CA2249409A CA2249409A1 CA 2249409 A1 CA2249409 A1 CA 2249409A1 CA 002249409 A CA002249409 A CA 002249409A CA 2249409 A CA2249409 A CA 2249409A CA 2249409 A1 CA2249409 A1 CA 2249409A1
- Authority
- CA
- Canada
- Prior art keywords
- amino acid
- seq
- peptide
- positions
- acid residue
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract 24
- 108010002231 IgA-specific serine endopeptidase Proteins 0.000 title abstract 2
- 239000012634 fragment Substances 0.000 title abstract 2
- 150000001413 amino acids Chemical class 0.000 claims abstract 19
- 125000000539 amino acid group Chemical group 0.000 claims abstract 18
- 150000004676 glycans Chemical class 0.000 claims abstract 10
- 239000005017 polysaccharide Substances 0.000 claims abstract 10
- 229920001282 polysaccharide Polymers 0.000 claims abstract 9
- 238000000034 method Methods 0.000 claims abstract 8
- 229960005486 vaccine Drugs 0.000 claims abstract 2
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 claims 6
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims 4
- -1 9-fluorenylmethyloxycarbonyl (Fmoc) groups Chemical group 0.000 claims 3
- 235000001014 amino acid Nutrition 0.000 claims 3
- 229940024606 amino acid Drugs 0.000 claims 3
- 125000003277 amino group Chemical group 0.000 claims 3
- JGFZNNIVVJXRND-UHFFFAOYSA-N N,N-Diisopropylethylamine (DIPEA) Chemical compound CCN(C(C)C)C(C)C JGFZNNIVVJXRND-UHFFFAOYSA-N 0.000 claims 2
- 241000588650 Neisseria meningitidis Species 0.000 claims 2
- NQRYJNQNLNOLGT-UHFFFAOYSA-N Piperidine Chemical compound C1CCNCC1 NQRYJNQNLNOLGT-UHFFFAOYSA-N 0.000 claims 2
- 230000008878 coupling Effects 0.000 claims 2
- 238000010168 coupling process Methods 0.000 claims 2
- 238000005859 coupling reaction Methods 0.000 claims 2
- 125000001841 imino group Chemical group [H]N=* 0.000 claims 2
- 238000003786 synthesis reaction Methods 0.000 claims 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims 1
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 claims 1
- 239000004475 Arginine Substances 0.000 claims 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims 1
- 239000004472 Lysine Substances 0.000 claims 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims 1
- 239000004473 Threonine Substances 0.000 claims 1
- 230000021736 acetylation Effects 0.000 claims 1
- 238000006640 acetylation reaction Methods 0.000 claims 1
- 230000004913 activation Effects 0.000 claims 1
- 239000000427 antigen Substances 0.000 claims 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims 1
- 235000009582 asparagine Nutrition 0.000 claims 1
- 229960001230 asparagine Drugs 0.000 claims 1
- 235000003704 aspartic acid Nutrition 0.000 claims 1
- 230000001580 bacterial effect Effects 0.000 claims 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims 1
- 230000001588 bifunctional effect Effects 0.000 claims 1
- 230000015572 biosynthetic process Effects 0.000 claims 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims 1
- 239000012050 conventional carrier Substances 0.000 claims 1
- 235000018417 cysteine Nutrition 0.000 claims 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims 1
- 239000003085 diluting agent Substances 0.000 claims 1
- 239000002158 endotoxin Substances 0.000 claims 1
- 239000012467 final product Substances 0.000 claims 1
- 125000000524 functional group Chemical group 0.000 claims 1
- 230000002538 fungal effect Effects 0.000 claims 1
- 235000013922 glutamic acid Nutrition 0.000 claims 1
- 239000004220 glutamic acid Substances 0.000 claims 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 claims 1
- 229920006008 lipopolysaccharide Polymers 0.000 claims 1
- 239000012528 membrane Substances 0.000 claims 1
- 239000000546 pharmaceutical excipient Substances 0.000 claims 1
- 150000004804 polysaccharides Polymers 0.000 claims 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims 1
- 235000004400 serine Nutrition 0.000 claims 1
- 239000007790 solid phase Substances 0.000 claims 1
- 125000003396 thiol group Chemical group [H]S* 0.000 claims 1
- 235000008521 threonine Nutrition 0.000 claims 1
- 125000002221 trityl group Chemical group [H]C1=C([H])C([H])=C([H])C([H])=C1C([*])(C1=C(C(=C(C(=C1[H])[H])[H])[H])[H])C1=C([H])C([H])=C([H])C([H])=C1[H] 0.000 claims 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims 1
- 235000002374 tyrosine Nutrition 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/385—Haptens or antigens, bound to carriers
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/60—Medicinal preparations containing antigens or antibodies characteristics by the carrier linked to the antigen
- A61K2039/6031—Proteins
- A61K2039/6037—Bacterial toxins, e.g. diphteria toxoid [DT], tetanus toxoid [TT]
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Zoology (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Animal Behavior & Ethology (AREA)
- Mycology (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Immunology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
- Detergent Compositions (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicinal Preparation (AREA)
Abstract
The present invention is concerned with a fragment of IgA1-protease having 40 to 200 amino acid residues and comprising at least 40 amino acids of an amino acid sequence as shown in SEQ ID NO 1, beginning with the amino acid in any one of positions 1 to 5 and ending with an amino acid in any one of positions 40 to 104 or a homologuous sequence, its use as a carrier for a conjugate, particularly in combination with a polysaccharide, and a process for producing the peptide as well as vaccines comprising said peptide.
Claims (25)
1. A peptide having 40 to 200 amino acid residues and comprising at least 40 amino acids of an amino acid sequence as shown in SEQ ID NO 1, beginning with the amino acid residue in any one of positions 1 to 5 and ending with an amino acid residue in any one of positions 40 to 104 or a homologuous sequence.
2. A peptide according to claim 1, comprising an amino acid sequence that is identical or homologous to an amino acid sequence selected from the group consisting of the amino acid sequences:
of SEQ ID NO 2, beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of positions 40 to 104;
of SEQ ID NO 3, beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of positions 40 to 104;
of SEQ ID NO 4, beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of positions 40 to 104; and of SEQ ID NO 5, beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of positions 40 to 104.
of SEQ ID NO 2, beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of positions 40 to 104;
of SEQ ID NO 3, beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of positions 40 to 104;
of SEQ ID NO 4, beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of positions 40 to 104; and of SEQ ID NO 5, beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of positions 40 to 104.
3. A peptide according to claim 1 or claim 2, comprising at least 40 amino acids having an amino acid sequence that is at least 85% identical to any one of the amino acid sequences of SEQ ID NO 1, SEQ ID NO 2, SEQ ID NO 3, SEQ ID NO 4, and SEQ ID
NO 5.
NO 5.
4. A peptide according to any one of the preceding claims, comprising at least 70 amino acid residues having an amino acid sequence that is identical or homologuous to an amino acid sequence of SEQ ID NO 1, SEQ ID NO 2, SEQ ID NO 3, SEQ ID NO 4, or SEQ ID NO 5 beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of the positions 70 to 104.
5. A peptide according to any one of the preceding claims, comprising at least 100 amino acid residues having an amino acid sequence that is identical or homologuous to an amino acid sequence of SEQ ID NO 1, SEQ ID NO 2, SEQ ID NO 3, SEQ ID NO 4, or SEQ ID NO 5 beginning with the amino acid residue in any one of positions 1 to 5 and ending with the amino acid residue in any one of the positions 100 to 104.
6. A peptide according claim 1, having the amino acid sequence of SEQ ID NO 1.
7. A peptide according to claim 1, comprising an amino acid sequence which is at least 85% identical to the amino acid sequence of SEQ ID NO 1.
8. A peptide according to anyone of the preceding claims, comprising additionally a cysteine residue.
9. A peptide according to claim 8, wherein the cysteine residue is located at one terminus of the peptide sequence.
10. Process for producing a peptide according to claim wherein an organic synthesis is used.
11. Process according to claim 10, wherein the synthesis is carried out using Fmoc or Boc chemistry and an automated peptide synthesizer.
12. Process according to claim 11, wherein FastMoc chemistry is used.
13. Process according to any one of claims 10 to 12, wherein the amino groups of the amino acids are protected with 9-fluorenylmethyloxycarbonyl (Fmoc) groups and side groups are protected with the following groups: the carboxyl or hydroxyl group, respectively, of aspartic acid, glutamic acid, serine, threonine and tyrosine with O-t-butyl; the amino or imino group, respectively, of histidine, asparagine and glutamine with trityl; the amino group of lysine with t-butyloxycarbonyl;
and the imino group of arginine with PMC and wherein the activation and coupling is done in the presence of HBTU/diiso-propylethylamine, and wherein the peptide is deprotected with piperidine and the final product is N-terminally acetylated using acetic anhydride.
and the imino group of arginine with PMC and wherein the activation and coupling is done in the presence of HBTU/diiso-propylethylamine, and wherein the peptide is deprotected with piperidine and the final product is N-terminally acetylated using acetic anhydride.
14. Process according to any one of claims 10 or 13, wherein double couplings and acetylation with acetic anhydride are used at cycles 1-2, 4, 10-13, 17, 27, 32, 49, 59, 66, 75-78, 84-85, 88, 96-97 and 104-105.
15. Process according to any one of claims 10 to 14, wherein the solid phase is TentaGel S RAM Spezial.
16. Process according to any one of claims 10 to 15, wherein a cysteine unit is added to the peptide at the N-terminus and/or the C-terminus.
17. Use of a peptide of any one of claims 1 to 9 as carrier for a conjugate.
18. Use of a peptide of any one of claims 1 to 9 as carrier for a polysaccharide selected from lipopolysaccharides, O-antigens, or bacterial, capsular or fungal membrane poly-saccharides.
19. Use of a peptide of any one of claims 1 to 9 as carrier for Polysaccharide C of Neisseria meningitidis.
20. Conjugate comprising a peptide according to any one of claims 1 to 9 and a immunoreactive molecule.
21. Conjugate according to claim 20, wherein the immunoreactive molecule is a polysaccharide.
22. Conjugate according to claim 20 or 21, comprising the peptide of any one of claims 1 to 9 with an additional cysteine residue, a bifunctional linker and a polysaccharide, wherein the peptide is bonded to the linker via the thiol group of the cysteine and the polysaccharide is bonded to the other functional group of the linker via a hydroxy, carboxy or amino group.
23. Conjugate according to any one of claims 20 to 22, wherein the polysaccharide is Polysaccharide C of Neisseria meningitidis.
24. Conjugate according to any one of claims 20 to 23, wherein one mole of peptide per 50 to 1 moles of repeating units of the polysaccharide is present.
25. Vaccine comprising the conjugate of any one of claims 20 to 24 together with conventional carriers, excipients and/or diluents.
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP97100883.4 | 1997-01-21 | ||
| EP97100883 | 1997-01-21 | ||
| PCT/EP1998/000294 WO1998031791A1 (en) | 1997-01-21 | 1998-01-20 | Iga1 protease fragment as carrier peptide |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2249409A1 true CA2249409A1 (en) | 1998-07-23 |
| CA2249409C CA2249409C (en) | 2010-10-26 |
Family
ID=8226386
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2249409A Expired - Fee Related CA2249409C (en) | 1997-01-21 | 1998-01-20 | Iga1 protease fragment as carrier peptide |
Country Status (14)
| Country | Link |
|---|---|
| US (1) | US7235242B2 (en) |
| EP (1) | EP0895537B1 (en) |
| JP (1) | JP2000507274A (en) |
| KR (1) | KR20000064740A (en) |
| AT (1) | ATE283914T1 (en) |
| AU (1) | AU6211698A (en) |
| CA (1) | CA2249409C (en) |
| DE (1) | DE69827880T2 (en) |
| DK (1) | DK0895537T3 (en) |
| ES (1) | ES2234095T3 (en) |
| NO (1) | NO322265B1 (en) |
| NZ (1) | NZ331968A (en) |
| PT (1) | PT895537E (en) |
| WO (1) | WO1998031791A1 (en) |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE19821859A1 (en) * | 1998-05-15 | 1999-12-09 | M Alexander Schmidt | Generation of immunogenic capsule polysaccharide-conjugates used to generate vaccines against Neisseria meningitidis |
| SG11201506885UA (en) | 2013-03-21 | 2015-09-29 | Sanofi Aventis Deutschland | Synthesis of cyclic imide containing peptide products |
| AU2014234400B2 (en) | 2013-03-21 | 2017-11-16 | Sanofi-Aventis Deutschland Gmbh | Synthesis of hydantoin containing peptide products |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3622221A1 (en) * | 1986-07-02 | 1988-01-14 | Max Planck Gesellschaft | METHOD FOR THE GENE-TECHNOLOGICAL EXTRACTION OF PROTEINS USING GRAM-NEGATIVE HOST CELLS |
| EP0326111A3 (en) * | 1988-01-29 | 1989-12-27 | New York Blood Center, Inc. | Peptide derivatives rendered immunogenic when administered with alum as an adjuvant |
| DK130889A (en) * | 1989-03-17 | 1990-09-18 | Mogens Kilian | IMMUNOGLOBULIN A1 PROTEASES (IGA1 PROTASES), PROCEDURES FOR GENTECHNOLOGICAL PREPARATION OF SUCH ENZYMES, AND VACCINE-CONTAINING ENZYMES AND SYMBOLS OF PROMISTS OF BACKGROUND IMMUNISTRY AND BIT |
| GB8924438D0 (en) * | 1989-10-31 | 1989-12-20 | Hoffmann La Roche | Vaccine composition |
-
1998
- 1998-01-20 AT AT98904105T patent/ATE283914T1/en active
- 1998-01-20 EP EP98904105A patent/EP0895537B1/en not_active Expired - Lifetime
- 1998-01-20 WO PCT/EP1998/000294 patent/WO1998031791A1/en active IP Right Grant
- 1998-01-20 DK DK98904105T patent/DK0895537T3/en active
- 1998-01-20 KR KR1019980707480A patent/KR20000064740A/en not_active Application Discontinuation
- 1998-01-20 ES ES98904105T patent/ES2234095T3/en not_active Expired - Lifetime
- 1998-01-20 NZ NZ331968A patent/NZ331968A/en not_active IP Right Cessation
- 1998-01-20 AU AU62116/98A patent/AU6211698A/en not_active Abandoned
- 1998-01-20 PT PT98904105T patent/PT895537E/en unknown
- 1998-01-20 DE DE69827880T patent/DE69827880T2/en not_active Expired - Lifetime
- 1998-01-20 CA CA2249409A patent/CA2249409C/en not_active Expired - Fee Related
- 1998-01-20 JP JP10533684A patent/JP2000507274A/en not_active Ceased
- 1998-09-18 NO NO19984365A patent/NO322265B1/en not_active IP Right Cessation
-
2004
- 2004-05-07 US US10/841,324 patent/US7235242B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| CA2249409C (en) | 2010-10-26 |
| DK0895537T3 (en) | 2005-03-29 |
| NO984365L (en) | 1998-11-19 |
| PT895537E (en) | 2005-04-29 |
| WO1998031791A1 (en) | 1998-07-23 |
| NZ331968A (en) | 1999-05-28 |
| DE69827880D1 (en) | 2005-01-05 |
| AU6211698A (en) | 1998-08-07 |
| EP0895537A1 (en) | 1999-02-10 |
| NO984365D0 (en) | 1998-09-18 |
| JP2000507274A (en) | 2000-06-13 |
| US7235242B2 (en) | 2007-06-26 |
| US20040203108A1 (en) | 2004-10-14 |
| ES2234095T3 (en) | 2005-06-16 |
| NO322265B1 (en) | 2006-09-04 |
| EP0895537B1 (en) | 2004-12-01 |
| DE69827880T2 (en) | 2005-11-03 |
| KR20000064740A (en) | 2000-11-06 |
| ATE283914T1 (en) | 2004-12-15 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| MKLA | Lapsed |
Effective date: 20150120 |